Searches of the MEROPS database

Display Known Cleavages for a Protein

Please enter a UniProt accession (eg P05067):

Accession:

Sequence Q53EL6

,


Click here to display alignment and conservation of cleavage sites of this sequence with close homologues.  This will take a few moments.

Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are not physiologically relevant are indicated by N. How cleavage sites have been identified are indicated by the following evidence codes: NT = N-terminal sequencing, MS = mass spectroscopy, MU = mutation, CS = consensus sequence, LC = liquid chromatography. To see all annotated cleavages for a peptidase, click on the peptidase name.

Cleavage Site Peptidase Residue range Cleavage type Description Evidence Reference
73 trypsin 1 1-469 N MS Schilling & Overall, 2008
86 trypsin 1 1-469 N MS Schilling & Overall, 2008
245 trypsin 1 1-469 N MS Schilling & Overall, 2008
256 trypsin 1 1-469 N MS Schilling & Overall, 2008
267 trypsin 1 1-469 N MS Schilling & Overall, 2008
283 trypsin 1 1-469 N MS Schilling & Overall, 2008
297 trypsin 1 1-469 N MS Schilling & Overall, 2008
306 trypsin 1 1-469 N MS Schilling & Overall, 2008
315 cathepsin S 312-329 N MS Biniossek et al., 2011
316 cathepsin L 312-329 N MS Biniossek et al., 2011
316 cathepsin S 312-329 N MS Biniossek et al., 2011
329 trypsin 1 1-469 N MS Schilling & Overall, 2008
336 trypsin 1 1-469 N MS Schilling & Overall, 2008
339 cathepsin B 337-352 N MS Biniossek et al., 2011
340 cathepsin L 337-352 N MS Biniossek et al., 2011
340 cathepsin S 337-352 N MS Biniossek et al., 2011
341 cathepsin L 337-352 N MS Biniossek et al., 2011